9QPU

Structure of human butyrylcholinesterase inhibited by the Ellman's reaction product, 2-[(3-carboxy-4-nitrophenyl)disulfanyl]ethyl-trimethylazanium

This is a non-PDB format compatible entry.

Entity

Entity ID	Chain ID	Description	Type	Chain length	Formula weight	Number of molecules	DB Name (Accession)	Biological source	Descriptive keywords
1	A (A)	Cholinesterase	polymer	529	59713.5	1	UniProt (P06276) Pfam (PF00135)	Homo sapiens (human)	Acylcholine acylhydrolase,Butyrylcholine esterase,Choline esterase II,Pseudocholinesterase
2	B (B)	alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose	branched		367.3	1	In PDB GlyTouCan (G86851RC)
3	C, D, E (C, D, E)	2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[alpha-L-fucopyranose-(1-6)]2-acetamido-2-deoxy-beta-D-glucopyranose	branched		570.5	3	In PDB GlyTouCan (G21290RB)
4	F, G (A)	2-acetamido-2-deoxy-beta-D-glucopyranose	non-polymer		221.2	2	Chemie (NAG)
5	H, L (A)	2-[(3-carboxy-4-nitro-phenyl)disulfanyl]ethyl-trimethyl-azanium	non-polymer		317.4	2	Chemie (A1I9A)
6	I, K, N (A)	2-(TRIMETHYLAMMONIUM)ETHYL THIOL	non-polymer		120.2	3	Chemie (ETM)
7	J, O, P (A)	GLYCEROL	non-polymer		92.1	3	Chemie (GOL)
8	M (A)	ACETATE ION	non-polymer		59.0	1	Chemie (ACT)
9	Q, R, S, T, U... (A)	SULFATE ION	non-polymer		96.1	9	Chemie (SO4)
10	Z (A)	SODIUM ION	non-polymer		23.0	1	Chemie (NA)
11	AA (A)	water	water		18.0	129	Chemie (HOH)

Sequence modifications

A: 1 - 529 (UniProt: P06276)

PDB	External Database	Details
Gln 17	Asn 45	engineered mutation
Gln 455	Asn 483	engineered mutation
Gln 481	Asn 509	engineered mutation
Gln 486	Asn 514	engineered mutation

Contents of the asymmetric unit

Polymers	Number of chains	1
	Total formula weight	59713.5
Branched	Number of molecules	4
	Total formula weight	2079.0
Non-Polymers*	Number of molecules	21
	Total formula weight	2660.8
All*	Total formula weight	64453.3

*Water molecules are not included.